1npx: Difference between revisions

Revision as of 15:09, 21 February 2008

STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION

OverviewOverview

The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.

About this StructureAbout this Structure

1NPX is a Single protein structure of sequence from Enterococcus faecalis with and as ligands. Active as NADH peroxidase, with EC number 1.11.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution., Stehle T, Ahmed SA, Claiborne A, Schulz GE, J Mol Biol. 1991 Oct 20;221(4):1325-44. PMID:1942054

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-[[Image:1npx.jpg|left|200px]]<br /><applet load="1npx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1npx.jpg|left|200px]]<br /><applet load="1npx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1npx, resolution 2.16&Aring;" />
 '''STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus, faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of, 2.16 A using the simulated annealing method. The final crystallographic, R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The, standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond, angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with, point group D2; the symmetry is crystallographic. The redox center of the, enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid, (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is, likely to act as an active-site base. In the analyzed crystal, the enzyme, was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid, Cys-SO3H. The chain fold of NADH peroxidase is similar to those of, disulfide oxidoreductases. A comparison with glutathione reductase, a, representative of this enzyme family, is given.
+The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.
 ==About this Structure==
-NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with CYO and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPX OCA].
+NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=CYO:'>CYO</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPX OCA].
 ==Reference==
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 [[Category: NADH peroxidase]]
 [[Category: Single protein]]
-[[Category: Ahmed, S.A.]]
+[[Category: Ahmed, S A.]]
 [[Category: Claiborne, A.]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: Stehle, T.]]
 [[Category: CYO]]
@@ Line 22: / Line 22: @@
 [[Category: oxidoreductase(h2o2(a))]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:28:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:49 2008''